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Literature summary for 1.11.1.17 extracted from

  • Vergauwen, B.; Pauwels, F.; Jacquemotte, F.; Meyer, T.E.; Cusanovich, M.A.; Bartsch, R.G.; van Beeumen, J.J.
    Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling (2001), J. Biol. Chem., 276, 20890-20897.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL(DE3) Marichromatium gracile

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of the glutathione amide reductase, using glutathione amide disulfide (cf. EC 1.8.1.16) and NADH as substrates Marichromatium gracile

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27430
-
calculated from the deduced amino acid sequence Marichromatium gracile
27500
-
chimeric enzyme composed of one N-terminal peroxidoxin-like domain followed by a glutaredoxin-like C-terminus, SDS-PAGE Marichromatium gracile

Organism

Organism UniProt Comment Textmining
Marichromatium gracile
-
-
-
Marichromatium gracile DSM 1712
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial purification of the Prx/Grx-containing crude extract, centrifugation, ammonium sulfate precipitation, butyl-Sepharose HR 16/10 column, dialysis, ResourceQ column Marichromatium gracile

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione amide + H2O2 similar acitivity with small alkyl hydroperoxides indicating broad substrate specificity Marichromatium gracile glutathione amide disulfide + H2O
-
?
glutathione amide + H2O2 similar acitivity with small alkyl hydroperoxides indicating broad substrate specificity Marichromatium gracile DSM 1712 glutathione amide disulfide + H2O
-
?

Synonyms

Synonyms Comment Organism
garB
-
Marichromatium gracile
More glutathione amide reductase, cf. EC 1.8.1.16 Marichromatium gracile
Prx-containing peroxidase
-
Marichromatium gracile
Prx/Grx chimeric enzyme peroxidoxin/glutaredoxin chimeric enzyme Marichromatium gracile

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Marichromatium gracile

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of the glutathione amide reductase, using glutathione amide disulfide (cf. EC 1.8.1.16) and NADH as substrates Marichromatium gracile

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
assay at Marichromatium gracile

Cofactor

Cofactor Comment Organism Structure
FAD
-
Marichromatium gracile

General Information

General Information Comment Organism
physiological function garB encodes the central enzyme in glutathione amide cycling. The enzyme is the first example of a prokaryotic low molecular mass thiol-dependent peroxidase. The hydroperoxide-dependent Prx/Grx-catalyzed oxidation of glutathione amide is established in vitro, and as to be expected, the reaction is fueled by NADH via glutathione amide redox recycling Marichromatium gracile

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of the glutathione amide reductase, using glutathione amide disulfide (cf. EC 1.8.1.16) and NADH as substrates Marichromatium gracile